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Article Abstract
Altemicidin and its analogs are valuable sulfonamide antibiotics with valuable antitumor and antibacterial activities. Structures of altemicidin and congeners feature an unusual sulfonamide side chain. In the biosynthesis of altemicidin, the aldehyde dehydrogenase SbzJ catalyzes the conversion of 2-sulfamoylacetic aldehyde into 2-sulfamoylacetic acid, a key step in producing the sulfonamide side chain. Here, we conducted the biochemical characterization and structure-function analysis of SbzJ. In vitro assays revealed that SbzJ exhibits substrate promiscuity, accepting various aldehyde substrates and cofactors. The crystal structure of SbzJ in complex with NAD, along with subsequent mutagenesis studies, provided insights into how SbzJ recognizes the sulfonamide group of the substrate. Notably, His431 and Glu240 were identified as key residues serving as catalytic bases to activate the catalytic Cys273 and a water molecule. These findings provide structural and mechanistic understanding of SbzJ, offering potential for enzyme engineering to generate novel bioactive compounds.
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